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Vitamins and Coenzymes, Part L
- 1st Edition, Volume 282 - September 24, 1997
- Editors: Donald B. McCormick, Edward A. Dennis, Melvin I. Simon, John W. Suttie, Conrad Wagner
- Language: English
- Hardback ISBN:9 7 8 - 0 - 1 2 - 1 8 2 1 8 3 - 8
- eBook ISBN:9 7 8 - 0 - 0 8 - 0 8 8 3 9 4 - 6
The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since… Read more
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Request a sales quoteThe critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. More than 270 volumes have been published (all of them still in print) and much of the material is relevant even today--truly an essential publication for researchers in all fields of life sciences.
- This volume and its companion Volumes 279, 280, and 281
- A collation of the most recent and useful methods for the identification, preparation, and quantification of vitamins and coenzymes
- Details on physical, chemical, and biological properties of vitamins and coenzymes
- Chemical and biological syntheses of vitamins, coenzymes, and their analogs
- Aspects of transport and metabolism of vitamins and coenzymes
Biochemists, nutritionists, cell biologists, pharmacologists, molecular biologists, and physiologists
Vitamin A:
A.W. Norris and E. Li, Generation and Characterization of Cellular Retinoic Acid-Binding Proteins from Escherichia coli Expression System.
M. Clagett-Dame and J.J. Repa, Generating and Characterizing Retinoid Receptors from Escherichia coli and Insect Cell Expression Systems.
E.A. Allegretto and R.A. Heyman, Expression and Characterization of Retinoid Receptors in Yeast.
A. Rowe and P.M. Brickell, Use of in Situ Hybridization Techniques to Study Embryonic Expression of Retinoid Receptors and Binding Proteins.
N. Ferrari, G. Vidali, and U. Pfeffer, Use of Quantitative PCR to Study Retinoid Receptor Expression.
L. Zhou, G. Otulakowski, and C.Y. Lau, Use of Quantitative PCR to Study Cellular Retinoic Acid Binding Protein-II mRNA Expression in Human Skin.
L. Wojnowski and A. Zimmer, Use of Transgenic Mice to Study Activation of Retinoic Acid-Responsive Promoters.
M. Saitou, T. Tanaka, and A. Kakizuka, Use of Transgenic Mice to Eliminate Retinoic Acid Receptor Function in Specific Tissues.
M. Wagner, Use of Reporter Cells to Study Endogenous Retinoid Sources in Embryonic Tissues.
P.K. Tadikonda and H.F. DeLuca, Preparation of Radiolabeled9-cis- and all-trans-Retinoids.
X-D. Wang and N.I. Krinsky, Identification and Quantification of Retinoic Acid and Other Metabolites from (-Carotene Excentric Cleavage in Human Intestine in Vitro and Ferret Intestine in Vivo.
R.S. Parker, J.T. Brenna, J.E. Swanson, K.J. Goodman, and B. Marmor, Assessing Metabolism of (-[13C] Carotene Using High Precision Isotope Ratio Mass Spectrometry. G. Tang, B.A. Andrien, G.G. Donikowski, and R.M. Russell, Atmospheric Pressure Chemical Ionization and Electron Capture Negative Chemical Ionization Mass Spectrometry in Studying (-Carotene Conversion to Retinol in Humans.
Vitamin D:
R. Ray and M.F. Holick, Synthesis of [3(-3H]Vitamin D3 and 1(,25-Dihydroxy[1(-3H]Vitamin D3.
M.J. Beckman and H.F. DeLuca, Assay of 1,25-Dihydroxyvitamin D3 from Serum Samples: Use of Receptor Binding or Enzyme Coupled Reporter Analysis.
B.W. Hollis, Quantitation of 25-Hydroxyvitamin D and 1,25-Dihydroxyvitamin D by Radioimmunoassay Using Radioiodinated Tracers.
Y. Ohyama, S-I. Hayashi, E. Usui, M. Noshiro, and K-I. Okuda, Assay of Vitamin D Derivatives and Purification of Vitamin D Hydroxylases.
M.J. Beckman and H.F. DeLuca, Assay of25-Hydroxyvitamin D 1(-Hydroxylase and 24-Hydroxylase.
M. Noshiro, Y. Ohyama, E. Usui, M. Akiyoshi-Shibata, Y. Yabusaki, and K-I. Okuda, Molecular Cloning of Vitamin D3 Hydroxylases.
T. Suda, E. Jimi, I. Nakamura, and N. Takahashi, Role of 1(,25-Dihydroxyvitamin D3 in Osteoclast Differentiation and Function.
J.G. Meszaros and M.C. Farach-Carson, Assay of Direct Effect of 1,25-Dihydroxyvitamin D3 on Calcium Ion Influx into Cultured Osteoblasts.
Vitamin E:
A. Beharka, S. Redican, L. Leka, and S.N. Meydani, Vitamin E Status and Immune Function.
M. Steiner, Inhibition of Platelet Adhesion as Functional Test for Vitamin E Status.
N. Noguchi and E. Niki, Inhibition of Plasma Cholesterol Ester Hydroperoxide and Phosphatidylcholine Hydroperoxide Formation as Measures of Antioxidant Status.
A.K. Dutta-Roy, (-Tocopherol-Binding Proteins: Purification and Characterization.
M. Schultz, M. Leist, A. Elsner, and R. Brigelius-Flohe, (-Carboxyethyl-6-hydroxychroman as Urinary Metabolite of Vitamin E.
Vitamin K:
K.L. Berkner and B.A. McNally, Purification of Vitamin K-Dependent Carboxylase from Cultured Cells.
B.C. Furie, A. Kuliopulos, D.A. Roth, I. Sugiura, C.T. Walsh, and B. Furie, Purification of Native Bovine Carboxylase and Expression and Purification of Recombinant Bovine Carboxylase.
S-M. Wu, V.P. Mutucumarana, and D.W. Stafford, Purification of (-Glutamyl Carboxylase from Bovine Liver.
R.J.T.J. Houben, B.A.M. Soute,and C. Vermeer, Assay of Vitamin K-Dependent Carboxylase Activity in Hepatic and Extrahepatic Tissues.
F.J. Castellino and J-P. Geng, Expression of Human Anticoagulation Protein C and (-Carboxyglutamic Acid Mutants in Mammalian Cell Cultures.
M.E. Benton and J.W. Suttie, Determination of Site-Specific (-Carboxyglutamic Formation by Vitamin K-Dependent Carboxylase Utilizing De-(-Carboxy Bone Gla Protein as Substrate.
R. Wallin and T.M. Guenthner, Purification of Warfarin-Sensitive Vitamin K Epoxide Reductase.
K.W. Davidson and J.A. Sadowski, Determination of Vitamin K Compounds in Plasma or Serum by High-Performance Liquid Chromatography Using Postcolumn Chemical Reduction and Fluorimetric Detection.
P.T. McCarthy, D.L. Harrington, and M.J. Shearer, Assay of Phylloquinone in Plasma by High-Performance Liquid Chromatography with Electrochemical Detection.
S.J. Hodges, Assay of Menaquinones in Plasma Utilizing Dual-Electrode Electrochemical Detection.
Y. Usui, Assay of Phylloquinone and Menaquinones in Human Liver.
S.L. Booth and J.A. Sadowski, Determination of Phylloquinone in Foods by High-Performance Liquid Chromatography.
J.M. Conly, Assay of Menaquinones in Bacterial Cultures, Stool Samples, and Intestinal Cultures.
Author Index.
Subject Index.
A.W. Norris and E. Li, Generation and Characterization of Cellular Retinoic Acid-Binding Proteins from Escherichia coli Expression System.
M. Clagett-Dame and J.J. Repa, Generating and Characterizing Retinoid Receptors from Escherichia coli and Insect Cell Expression Systems.
E.A. Allegretto and R.A. Heyman, Expression and Characterization of Retinoid Receptors in Yeast.
A. Rowe and P.M. Brickell, Use of in Situ Hybridization Techniques to Study Embryonic Expression of Retinoid Receptors and Binding Proteins.
N. Ferrari, G. Vidali, and U. Pfeffer, Use of Quantitative PCR to Study Retinoid Receptor Expression.
L. Zhou, G. Otulakowski, and C.Y. Lau, Use of Quantitative PCR to Study Cellular Retinoic Acid Binding Protein-II mRNA Expression in Human Skin.
L. Wojnowski and A. Zimmer, Use of Transgenic Mice to Study Activation of Retinoic Acid-Responsive Promoters.
M. Saitou, T. Tanaka, and A. Kakizuka, Use of Transgenic Mice to Eliminate Retinoic Acid Receptor Function in Specific Tissues.
M. Wagner, Use of Reporter Cells to Study Endogenous Retinoid Sources in Embryonic Tissues.
P.K. Tadikonda and H.F. DeLuca, Preparation of Radiolabeled9-cis- and all-trans-Retinoids.
X-D. Wang and N.I. Krinsky, Identification and Quantification of Retinoic Acid and Other Metabolites from (-Carotene Excentric Cleavage in Human Intestine in Vitro and Ferret Intestine in Vivo.
R.S. Parker, J.T. Brenna, J.E. Swanson, K.J. Goodman, and B. Marmor, Assessing Metabolism of (-[13C] Carotene Using High Precision Isotope Ratio Mass Spectrometry. G. Tang, B.A. Andrien, G.G. Donikowski, and R.M. Russell, Atmospheric Pressure Chemical Ionization and Electron Capture Negative Chemical Ionization Mass Spectrometry in Studying (-Carotene Conversion to Retinol in Humans.
Vitamin D:
R. Ray and M.F. Holick, Synthesis of [3(-3H]Vitamin D3 and 1(,25-Dihydroxy[1(-3H]Vitamin D3.
M.J. Beckman and H.F. DeLuca, Assay of 1,25-Dihydroxyvitamin D3 from Serum Samples: Use of Receptor Binding or Enzyme Coupled Reporter Analysis.
B.W. Hollis, Quantitation of 25-Hydroxyvitamin D and 1,25-Dihydroxyvitamin D by Radioimmunoassay Using Radioiodinated Tracers.
Y. Ohyama, S-I. Hayashi, E. Usui, M. Noshiro, and K-I. Okuda, Assay of Vitamin D Derivatives and Purification of Vitamin D Hydroxylases.
M.J. Beckman and H.F. DeLuca, Assay of25-Hydroxyvitamin D 1(-Hydroxylase and 24-Hydroxylase.
M. Noshiro, Y. Ohyama, E. Usui, M. Akiyoshi-Shibata, Y. Yabusaki, and K-I. Okuda, Molecular Cloning of Vitamin D3 Hydroxylases.
T. Suda, E. Jimi, I. Nakamura, and N. Takahashi, Role of 1(,25-Dihydroxyvitamin D3 in Osteoclast Differentiation and Function.
J.G. Meszaros and M.C. Farach-Carson, Assay of Direct Effect of 1,25-Dihydroxyvitamin D3 on Calcium Ion Influx into Cultured Osteoblasts.
Vitamin E:
A. Beharka, S. Redican, L. Leka, and S.N. Meydani, Vitamin E Status and Immune Function.
M. Steiner, Inhibition of Platelet Adhesion as Functional Test for Vitamin E Status.
N. Noguchi and E. Niki, Inhibition of Plasma Cholesterol Ester Hydroperoxide and Phosphatidylcholine Hydroperoxide Formation as Measures of Antioxidant Status.
A.K. Dutta-Roy, (-Tocopherol-Binding Proteins: Purification and Characterization.
M. Schultz, M. Leist, A. Elsner, and R. Brigelius-Flohe, (-Carboxyethyl-6-hydroxychroman as Urinary Metabolite of Vitamin E.
Vitamin K:
K.L. Berkner and B.A. McNally, Purification of Vitamin K-Dependent Carboxylase from Cultured Cells.
B.C. Furie, A. Kuliopulos, D.A. Roth, I. Sugiura, C.T. Walsh, and B. Furie, Purification of Native Bovine Carboxylase and Expression and Purification of Recombinant Bovine Carboxylase.
S-M. Wu, V.P. Mutucumarana, and D.W. Stafford, Purification of (-Glutamyl Carboxylase from Bovine Liver.
R.J.T.J. Houben, B.A.M. Soute,and C. Vermeer, Assay of Vitamin K-Dependent Carboxylase Activity in Hepatic and Extrahepatic Tissues.
F.J. Castellino and J-P. Geng, Expression of Human Anticoagulation Protein C and (-Carboxyglutamic Acid Mutants in Mammalian Cell Cultures.
M.E. Benton and J.W. Suttie, Determination of Site-Specific (-Carboxyglutamic Formation by Vitamin K-Dependent Carboxylase Utilizing De-(-Carboxy Bone Gla Protein as Substrate.
R. Wallin and T.M. Guenthner, Purification of Warfarin-Sensitive Vitamin K Epoxide Reductase.
K.W. Davidson and J.A. Sadowski, Determination of Vitamin K Compounds in Plasma or Serum by High-Performance Liquid Chromatography Using Postcolumn Chemical Reduction and Fluorimetric Detection.
P.T. McCarthy, D.L. Harrington, and M.J. Shearer, Assay of Phylloquinone in Plasma by High-Performance Liquid Chromatography with Electrochemical Detection.
S.J. Hodges, Assay of Menaquinones in Plasma Utilizing Dual-Electrode Electrochemical Detection.
Y. Usui, Assay of Phylloquinone and Menaquinones in Human Liver.
S.L. Booth and J.A. Sadowski, Determination of Phylloquinone in Foods by High-Performance Liquid Chromatography.
J.M. Conly, Assay of Menaquinones in Bacterial Cultures, Stool Samples, and Intestinal Cultures.
Author Index.
Subject Index.
- No. of pages: 505
- Language: English
- Edition: 1
- Volume: 282
- Published: September 24, 1997
- Imprint: Academic Press
- Hardback ISBN: 9780121821838
- eBook ISBN: 9780080883946
DM
Donald B. McCormick
Affiliations and expertise
Emory University, Atlanta, Georgia, U.S.A.ED
Edward A. Dennis
Edward A. Dennis: University of California, San Diego Distinguished Professor of Chemistry and Biochemistry and former Department Chair and Professor of Pharmacology in the School of Medicine, Dennis is currently Editor-in-Chief of the Journal of Lipid Research and Director of the LIPID MAPS initiative. He also served as Chair of the Board of Directors of the Keystone Symposia on Molecular and Cellular Biology and current as an Emeritus member of the Board of Directors. His current research focus is on phospholipases, cell signaling and lipidomics on which he has published over 300 papers, most related to signal transduction by lipid messengers
Affiliations and expertise
University of California at San Diego, La Jolla, CA, U.S.A.MS
Melvin I. Simon
Affiliations and expertise
The Salk Institute, La Jolla, CA, USAJS
John W. Suttie
Affiliations and expertise
University of Wisconsin, Madison, U.S.A.CW
Conrad Wagner
Affiliations and expertise
Department of Veterans Affairs Medical Center and Vanderbilt University, Nashville, Tennessee, U.S.A.Read Vitamins and Coenzymes, Part L on ScienceDirect